Literature DB >> 3072021

Gene sequence and primary structure of mitochondrial malate dehydrogenase from Saccharomyces cerevisiae.

L M Thompson1, P Sutherland, J S Steffan, L McAlister-Henn.   

Abstract

The nucleotide sequence was determined for a 1.5-kilobase genomic fragment containing the mitochondrial malate dehydrogenase gene (MDH1) of Saccharomyces cerevisiae. The open-reading frame encodes a precursor form of the mature enzyme containing an amino-terminal extension of 17 amino acid residues. In vitro translation experiments confirm that the initial translation product of MDH1 is larger than the mature polypeptide. Transcription of MDH1 initiates at several sites from 83 to 97 nucleotides 5' of the translational start site. Alignment of the amino acid sequence for the mature yeast enzyme with those for mammalian mitochondrial and for Escherichia coli malate dehydrogenases reveals polypeptides of very similar sizes with identical amino acids at 54% and 48% of the residue positions, respectively. The amino acid sequences of the yeast and mammalian mitochondrial targeting sequences are similar but less related than the mature polypeptides. The yeast MDH1 gene is shown to reside on chromosome XI.

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Year:  1988        PMID: 3072021     DOI: 10.1021/bi00422a015

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  12 in total

1.  Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor protein.

Authors:  C Gietl; M Lehnerer; O Olsen
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2.  Nucleotide sequence of a cDNA encoding mitochondrial malate dehydrogenase from Eucalyptus.

Authors:  O Poeydomenge; M Marolda; A M Boudet; J Grima-Pettenati
Journal:  Plant Physiol       Date:  1995-04       Impact factor: 8.340

Review 3.  PET genes of Saccharomyces cerevisiae.

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Journal:  Microbiol Rev       Date:  1990-09

4.  Effects of excess succinate and retrograde control of metabolite accumulation in yeast tricarboxylic cycle mutants.

Authors:  An-Ping Lin; Sondra L Anderson; Karyl I Minard; Lee McAlister-Henn
Journal:  J Biol Chem       Date:  2011-08-12       Impact factor: 5.157

5.  The mitochondrial alcohol dehydrogenase Adh3p is involved in a redox shuttle in Saccharomyces cerevisiae.

Authors:  B M Bakker; C Bro; P Kötter; M A Luttik; J P van Dijken; J T Pronk
Journal:  J Bacteriol       Date:  2000-09       Impact factor: 3.490

6.  The malate-aspartate NADH shuttle components are novel metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast.

Authors:  Erin Easlon; Felicia Tsang; Craig Skinner; Chen Wang; Su-Ju Lin
Journal:  Genes Dev       Date:  2008-04-01       Impact factor: 11.361

7.  Redox responses in yeast to acetate as the carbon source.

Authors:  Karyl I Minard; L McAlister-Henn
Journal:  Arch Biochem Biophys       Date:  2008-12-30       Impact factor: 4.013

8.  Disulfide bond formation in yeast NAD+-specific isocitrate dehydrogenase.

Authors:  Joshua A Garcia; Karyl I Minard; An-Ping Lin; Lee McAlister-Henn
Journal:  Biochemistry       Date:  2009-09-22       Impact factor: 3.162

9.  Isolation, nucleotide sequence analysis, and disruption of the MDH2 gene from Saccharomyces cerevisiae: evidence for three isozymes of yeast malate dehydrogenase.

Authors:  K I Minard; L McAlister-Henn
Journal:  Mol Cell Biol       Date:  1991-01       Impact factor: 4.272

10.  Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization.

Authors:  F-Nora Vögtle; Claudia Prinz; Josef Kellermann; Friedrich Lottspeich; Nikolaus Pfanner; Chris Meisinger
Journal:  Mol Biol Cell       Date:  2011-04-27       Impact factor: 4.138

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